A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species

J Gen Virol. 2006 Dec;87(Pt 12):3649-53. doi: 10.1099/vir.0.82261-0.

Abstract

The V protein of the paramyxovirus Nipah virus (NiV) has been shown to antagonize the interferon (IFN) response in human cells via sequestration of STAT1 and STAT2. This study describes a mutant of the NiV V protein, referred to as V(AAHL), that is unable to antagonize IFN signalling and demonstrates that a single amino acid substitution is responsible for its inactivity. The molecular basis for this was identified as a failure to interact with STAT1 and STAT2. It was also shown that NiV V, but not V(AAHL), was functional as an IFN antagonist in human, monkey, rabbit, dog, horse, pig and bat cells, which suggests that the ability of NiV to block IFN signalling is not a major constraint that prevents this virus from crossing species barriers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution*
  • Genes, Reporter
  • Interferons / antagonists & inhibitors*
  • Interferons / metabolism
  • Luciferases / analysis
  • Luciferases / genetics
  • Mutation
  • Nipah Virus / genetics*
  • Nipah Virus / immunology*
  • Protein Binding
  • STAT1 Transcription Factor / metabolism
  • STAT2 Transcription Factor / metabolism
  • Viral Proteins / genetics*
  • Viral Proteins / metabolism
  • Viral Proteins / physiology*

Substances

  • STAT1 Transcription Factor
  • STAT1 protein, human
  • STAT2 Transcription Factor
  • STAT2 protein, human
  • Viral Proteins
  • Interferons
  • Luciferases